JP2957695B2 - 組み換えタンパク質の回収法 - Google Patents
組み換えタンパク質の回収法Info
- Publication number
- JP2957695B2 JP2957695B2 JP2507613A JP50761390A JP2957695B2 JP 2957695 B2 JP2957695 B2 JP 2957695B2 JP 2507613 A JP2507613 A JP 2507613A JP 50761390 A JP50761390 A JP 50761390A JP 2957695 B2 JP2957695 B2 JP 2957695B2
- Authority
- JP
- Japan
- Prior art keywords
- protein
- molecular weight
- solution
- recombinant
- group
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Expired - Fee Related
Links
- 238000000034 method Methods 0.000 title claims abstract description 55
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 title claims abstract description 52
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 title claims abstract description 52
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 128
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 128
- 239000000243 solution Substances 0.000 claims abstract description 41
- 150000001412 amines Chemical class 0.000 claims abstract description 22
- 150000003856 quaternary ammonium compounds Chemical class 0.000 claims abstract description 19
- 239000012460 protein solution Substances 0.000 claims abstract description 18
- 239000002244 precipitate Substances 0.000 claims abstract description 16
- 108010051696 Growth Hormone Proteins 0.000 claims description 42
- 102000018997 Growth Hormone Human genes 0.000 claims description 29
- 239000000122 growth hormone Substances 0.000 claims description 27
- 229910052739 hydrogen Inorganic materials 0.000 claims description 15
- 239000001257 hydrogen Substances 0.000 claims description 15
- UFHFLCQGNIYNRP-UHFFFAOYSA-N Hydrogen Chemical compound [H][H] UFHFLCQGNIYNRP-UHFFFAOYSA-N 0.000 claims description 14
- 125000000217 alkyl group Chemical group 0.000 claims description 13
- 125000000547 substituted alkyl group Chemical group 0.000 claims description 11
- 150000001450 anions Chemical group 0.000 claims description 9
- DDXLVDQZPFLQMZ-UHFFFAOYSA-M dodecyl(trimethyl)azanium;chloride Chemical compound [Cl-].CCCCCCCCCCCC[N+](C)(C)C DDXLVDQZPFLQMZ-UHFFFAOYSA-M 0.000 claims description 9
- 125000002947 alkylene group Chemical group 0.000 claims description 8
- 125000000732 arylene group Chemical group 0.000 claims description 8
- 238000001556 precipitation Methods 0.000 claims description 8
- IZBZQUREHISXFJ-UHFFFAOYSA-N 2-[4-chloro-5-methyl-3-(trifluoromethyl)pyrazol-1-yl]acetic acid Chemical compound CC1=C(Cl)C(C(F)(F)F)=NN1CC(O)=O IZBZQUREHISXFJ-UHFFFAOYSA-N 0.000 claims description 6
- CPELXLSAUQHCOX-UHFFFAOYSA-M Bromide Chemical group [Br-] CPELXLSAUQHCOX-UHFFFAOYSA-M 0.000 claims description 6
- 150000001242 acetic acid derivatives Chemical class 0.000 claims description 5
- 229910052799 carbon Inorganic materials 0.000 claims description 5
- 150000001805 chlorine compounds Chemical group 0.000 claims description 5
- 150000002823 nitrates Chemical class 0.000 claims description 5
- 241000283690 Bos taurus Species 0.000 claims description 4
- VEXZGXHMUGYJMC-UHFFFAOYSA-M Chloride anion Chemical compound [Cl-] VEXZGXHMUGYJMC-UHFFFAOYSA-M 0.000 claims description 4
- QAOWNCQODCNURD-UHFFFAOYSA-L Sulfate Chemical group [O-]S([O-])(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-L 0.000 claims description 4
- 241000282414 Homo sapiens Species 0.000 claims description 3
- WOWHHFRSBJGXCM-UHFFFAOYSA-M cetyltrimethylammonium chloride Chemical compound [Cl-].CCCCCCCCCCCCCCCC[N+](C)(C)C WOWHHFRSBJGXCM-UHFFFAOYSA-M 0.000 claims description 3
- LQEXPHILFYMEJR-UHFFFAOYSA-N methylazanium dichloride Chemical compound Cl.Cl.NC.NC LQEXPHILFYMEJR-UHFFFAOYSA-N 0.000 claims description 3
- 241001494479 Pecora Species 0.000 claims description 2
- VBIIFPGSPJYLRR-UHFFFAOYSA-M Stearyltrimethylammonium chloride Chemical compound [Cl-].CCCCCCCCCCCCCCCCCC[N+](C)(C)C VBIIFPGSPJYLRR-UHFFFAOYSA-M 0.000 claims description 2
- 239000003760 tallow Substances 0.000 claims description 2
- NLXLAEXVIDQMFP-UHFFFAOYSA-N Ammonia chloride Chemical compound [NH4+].[Cl-] NLXLAEXVIDQMFP-UHFFFAOYSA-N 0.000 claims 4
- 235000019270 ammonium chloride Nutrition 0.000 claims 2
- UPAYMTNRIUMDBC-UHFFFAOYSA-N azane 1-chloro-18,18-dimethylnonadecane Chemical compound N.CC(C)(C)CCCCCCCCCCCCCCCCCCl UPAYMTNRIUMDBC-UHFFFAOYSA-N 0.000 claims 1
- XMBWDFGMSWQBCA-UHFFFAOYSA-N hydrogen iodide Chemical group I XMBWDFGMSWQBCA-UHFFFAOYSA-N 0.000 claims 1
- 125000001273 sulfonato group Chemical group [O-]S(*)(=O)=O 0.000 claims 1
- 239000000356 contaminant Substances 0.000 abstract description 30
- 239000000203 mixture Substances 0.000 abstract description 2
- 238000011084 recovery Methods 0.000 description 21
- 210000003000 inclusion body Anatomy 0.000 description 17
- 102100038803 Somatotropin Human genes 0.000 description 13
- -1 precipitants Substances 0.000 description 11
- 229920000642 polymer Polymers 0.000 description 10
- 238000000926 separation method Methods 0.000 description 9
- 238000004587 chromatography analysis Methods 0.000 description 8
- 150000001875 compounds Chemical class 0.000 description 8
- 244000005700 microbiome Species 0.000 description 8
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 7
- 239000003398 denaturant Substances 0.000 description 7
- 239000000047 product Substances 0.000 description 7
- 108010006025 bovine growth hormone Proteins 0.000 description 6
- 210000004027 cell Anatomy 0.000 description 6
- 239000003153 chemical reaction reagent Substances 0.000 description 5
- 239000003599 detergent Substances 0.000 description 5
- 238000005227 gel permeation chromatography Methods 0.000 description 5
- 238000004519 manufacturing process Methods 0.000 description 5
- 239000012528 membrane Substances 0.000 description 5
- 230000000813 microbial effect Effects 0.000 description 5
- 239000006228 supernatant Substances 0.000 description 5
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 4
- 150000001413 amino acids Chemical group 0.000 description 4
- 238000007796 conventional method Methods 0.000 description 4
- 230000002068 genetic effect Effects 0.000 description 4
- NOESYZHRGYRDHS-UHFFFAOYSA-N insulin Chemical compound N1C(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(NC(=O)CN)C(C)CC)CSSCC(C(NC(CO)C(=O)NC(CC(C)C)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CCC(N)=O)C(=O)NC(CC(C)C)C(=O)NC(CCC(O)=O)C(=O)NC(CC(N)=O)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CSSCC(NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2C=CC(O)=CC=2)NC(=O)C(CC(C)C)NC(=O)C(C)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2NC=NC=2)NC(=O)C(CO)NC(=O)CNC2=O)C(=O)NCC(=O)NC(CCC(O)=O)C(=O)NC(CCCNC(N)=N)C(=O)NCC(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC(O)=CC=3)C(=O)NC(C(C)O)C(=O)N3C(CCC3)C(=O)NC(CCCCN)C(=O)NC(C)C(O)=O)C(=O)NC(CC(N)=O)C(O)=O)=O)NC(=O)C(C(C)CC)NC(=O)C(CO)NC(=O)C(C(C)O)NC(=O)C1CSSCC2NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(N)CC=1C=CC=CC=1)C(C)C)CC1=CN=CN1 NOESYZHRGYRDHS-UHFFFAOYSA-N 0.000 description 4
- 239000013612 plasmid Substances 0.000 description 4
- 241000588724 Escherichia coli Species 0.000 description 3
- 108090000723 Insulin-Like Growth Factor I Proteins 0.000 description 3
- 230000008901 benefit Effects 0.000 description 3
- 125000004432 carbon atom Chemical group C* 0.000 description 3
- 238000005119 centrifugation Methods 0.000 description 3
- 239000003638 chemical reducing agent Substances 0.000 description 3
- 239000000539 dimer Substances 0.000 description 3
- 238000004128 high performance liquid chromatography Methods 0.000 description 3
- 238000001155 isoelectric focusing Methods 0.000 description 3
- 238000000746 purification Methods 0.000 description 3
- 150000003871 sulfonates Chemical class 0.000 description 3
- 238000012360 testing method Methods 0.000 description 3
- BMVXCPBXGZKUPN-UHFFFAOYSA-N 1-hexanamine Chemical compound CCCCCCN BMVXCPBXGZKUPN-UHFFFAOYSA-N 0.000 description 2
- 102000004877 Insulin Human genes 0.000 description 2
- 108090001061 Insulin Proteins 0.000 description 2
- 125000001429 N-terminal alpha-amino-acid group Chemical group 0.000 description 2
- 108010034634 Repressor Proteins Proteins 0.000 description 2
- 102000009661 Repressor Proteins Human genes 0.000 description 2
- 102000013275 Somatomedins Human genes 0.000 description 2
- 230000004071 biological effect Effects 0.000 description 2
- 238000006243 chemical reaction Methods 0.000 description 2
- 238000000502 dialysis Methods 0.000 description 2
- 230000000694 effects Effects 0.000 description 2
- 238000001914 filtration Methods 0.000 description 2
- 238000007429 general method Methods 0.000 description 2
- REYJJPSVUYRZGE-UHFFFAOYSA-O hydron;octadecan-1-amine Chemical compound CCCCCCCCCCCCCCCCCC[NH3+] REYJJPSVUYRZGE-UHFFFAOYSA-O 0.000 description 2
- 230000006872 improvement Effects 0.000 description 2
- 239000012535 impurity Substances 0.000 description 2
- 229940125396 insulin Drugs 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
- 239000000178 monomer Substances 0.000 description 2
- 239000007800 oxidant agent Substances 0.000 description 2
- 238000000159 protein binding assay Methods 0.000 description 2
- 230000007928 solubilization Effects 0.000 description 2
- 238000005063 solubilization Methods 0.000 description 2
- 239000002904 solvent Substances 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- BDHFUVZGWQCTTF-UHFFFAOYSA-M sulfonate Chemical compound [O-]S(=O)=O BDHFUVZGWQCTTF-UHFFFAOYSA-M 0.000 description 2
- 150000003467 sulfuric acid derivatives Chemical group 0.000 description 2
- QTBSBXVTEAMEQO-UHFFFAOYSA-M Acetate Chemical compound CC([O-])=O QTBSBXVTEAMEQO-UHFFFAOYSA-M 0.000 description 1
- 241000271566 Aves Species 0.000 description 1
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical group [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 1
- 102100021809 Chorionic somatomammotropin hormone 1 Human genes 0.000 description 1
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 1
- MYMOFIZGZYHOMD-UHFFFAOYSA-N Dioxygen Chemical compound O=O MYMOFIZGZYHOMD-UHFFFAOYSA-N 0.000 description 1
- SNRUBQQJIBEYMU-UHFFFAOYSA-N Dodecane Natural products CCCCCCCCCCCC SNRUBQQJIBEYMU-UHFFFAOYSA-N 0.000 description 1
- 241000196324 Embryophyta Species 0.000 description 1
- 241001131785 Escherichia coli HB101 Species 0.000 description 1
- 241000701959 Escherichia virus Lambda Species 0.000 description 1
- 241000702189 Escherichia virus Mu Species 0.000 description 1
- 102100037852 Insulin-like growth factor I Human genes 0.000 description 1
- 108010050904 Interferons Proteins 0.000 description 1
- 102000014150 Interferons Human genes 0.000 description 1
- 108010063738 Interleukins Proteins 0.000 description 1
- 102000015696 Interleukins Human genes 0.000 description 1
- 229910002651 NO3 Inorganic materials 0.000 description 1
- NHNBFGGVMKEFGY-UHFFFAOYSA-N Nitrate Chemical compound [O-][N+]([O-])=O NHNBFGGVMKEFGY-UHFFFAOYSA-N 0.000 description 1
- 108010003044 Placental Lactogen Proteins 0.000 description 1
- 239000000381 Placental Lactogen Substances 0.000 description 1
- 108010057464 Prolactin Proteins 0.000 description 1
- 102100024819 Prolactin Human genes 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- 108010056088 Somatostatin Proteins 0.000 description 1
- 102000005157 Somatostatin Human genes 0.000 description 1
- 239000004809 Teflon Substances 0.000 description 1
- 229920006362 Teflon® Polymers 0.000 description 1
- 230000004913 activation Effects 0.000 description 1
- 239000003957 anion exchange resin Substances 0.000 description 1
- 239000003054 catalyst Substances 0.000 description 1
- 150000001768 cations Chemical class 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 238000010276 construction Methods 0.000 description 1
- 238000012258 culturing Methods 0.000 description 1
- 229910001882 dioxygen Inorganic materials 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 229960000789 guanidine hydrochloride Drugs 0.000 description 1
- PJJJBBJSCAKJQF-UHFFFAOYSA-N guanidinium chloride Chemical compound [Cl-].NC(N)=[NH2+] PJJJBBJSCAKJQF-UHFFFAOYSA-N 0.000 description 1
- 239000010903 husk Substances 0.000 description 1
- 150000002431 hydrogen Chemical class 0.000 description 1
- 125000004435 hydrogen atom Chemical group [H]* 0.000 description 1
- 230000001939 inductive effect Effects 0.000 description 1
- 239000002198 insoluble material Substances 0.000 description 1
- 229940079322 interferon Drugs 0.000 description 1
- 238000005342 ion exchange Methods 0.000 description 1
- 150000002500 ions Chemical class 0.000 description 1
- 150000002632 lipids Chemical class 0.000 description 1
- 239000000155 melt Substances 0.000 description 1
- 238000005374 membrane filtration Methods 0.000 description 1
- 229910052751 metal Inorganic materials 0.000 description 1
- 239000002184 metal Substances 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 229940097325 prolactin Drugs 0.000 description 1
- 230000006920 protein precipitation Effects 0.000 description 1
- 238000001742 protein purification Methods 0.000 description 1
- 239000011347 resin Substances 0.000 description 1
- 229920005989 resin Polymers 0.000 description 1
- 102220201851 rs143406017 Human genes 0.000 description 1
- 125000003607 serino group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C(O[H])([H])[H] 0.000 description 1
- HAEPBEMBOAIUPN-UHFFFAOYSA-L sodium tetrathionate Chemical compound O.O.[Na+].[Na+].[O-]S(=O)(=O)SSS([O-])(=O)=O HAEPBEMBOAIUPN-UHFFFAOYSA-L 0.000 description 1
- 230000003381 solubilizing effect Effects 0.000 description 1
- NHXLMOGPVYXJNR-ATOGVRKGSA-N somatostatin Chemical compound C([C@H]1C(=O)N[C@H](C(N[C@@H](CO)C(=O)N[C@@H](CSSC[C@@H](C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@@H](CC=2C3=CC=CC=C3NC=2)C(=O)N[C@@H](CCCCN)C(=O)N[C@H](C(=O)N1)[C@@H](C)O)NC(=O)CNC(=O)[C@H](C)N)C(O)=O)=O)[C@H](O)C)C1=CC=CC=C1 NHXLMOGPVYXJNR-ATOGVRKGSA-N 0.000 description 1
- 229960000553 somatostatin Drugs 0.000 description 1
- 241000894007 species Species 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 125000003396 thiol group Chemical group [H]S* 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 230000001131 transforming effect Effects 0.000 description 1
- 230000014616 translation Effects 0.000 description 1
- GPRLSGONYQIRFK-MNYXATJNSA-N triton Chemical compound [3H+] GPRLSGONYQIRFK-MNYXATJNSA-N 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/575—Hormones
- C07K14/61—Growth hormone [GH], i.e. somatotropin
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/14—Extraction; Separation; Purification
- C07K1/30—Extraction; Separation; Purification by precipitation
- C07K1/303—Extraction; Separation; Purification by precipitation by salting out
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Molecular Biology (AREA)
- Medicinal Chemistry (AREA)
- Endocrinology (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Toxicology (AREA)
- Gastroenterology & Hepatology (AREA)
- Zoology (AREA)
- Analytical Chemistry (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US07/364,846 US5101018A (en) | 1989-06-12 | 1989-06-12 | Method for recovering recombinant proteins |
| US364,846 | 1989-06-12 |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JPH04505706A JPH04505706A (ja) | 1992-10-08 |
| JP2957695B2 true JP2957695B2 (ja) | 1999-10-06 |
Family
ID=23436347
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2507613A Expired - Fee Related JP2957695B2 (ja) | 1989-06-12 | 1990-05-10 | 組み換えタンパク質の回収法 |
Country Status (14)
| Country | Link |
|---|---|
| US (1) | US5101018A (de) |
| EP (1) | EP0477198B1 (de) |
| JP (1) | JP2957695B2 (de) |
| KR (1) | KR0178274B1 (de) |
| AT (1) | ATE96805T1 (de) |
| AU (1) | AU634547B2 (de) |
| BR (1) | BR9007433A (de) |
| CA (1) | CA2060505C (de) |
| DE (1) | DE69004429T2 (de) |
| DK (1) | DK0477198T3 (de) |
| ES (1) | ES2046782T3 (de) |
| HU (2) | HU209651B (de) |
| RU (1) | RU2075509C1 (de) |
| WO (1) | WO1990015876A1 (de) |
Families Citing this family (9)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5047511A (en) * | 1989-08-28 | 1991-09-10 | Pitman-Moore, Inc. | Method for recovering recombinant proteins |
| US5605691A (en) * | 1992-09-17 | 1997-02-25 | Ophidian Pharmaceuticals, Inc. | Immunologically active proteins from inclusion bodies |
| US5869604A (en) * | 1995-11-09 | 1999-02-09 | Georgia Institute Of Technology | Crystallization and purification of polypeptides |
| US7611700B2 (en) * | 2002-09-09 | 2009-11-03 | Hanall Pharmaceuticals, Co., Ltd. | Protease resistant modified interferon alpha polypeptides |
| US7998930B2 (en) | 2004-11-04 | 2011-08-16 | Hanall Biopharma Co., Ltd. | Modified growth hormones |
| TWI504405B (zh) * | 2009-01-22 | 2015-10-21 | Novo Nordisk Healthcare Ag | 穩定的生長激素化合物 |
| CN102834109B (zh) | 2010-01-22 | 2016-01-20 | 诺沃—诺迪斯克保健股份有限公司 | 稳定的生长激素化合物 |
| RU2012134974A (ru) | 2010-01-22 | 2014-02-27 | Ново Нордиск Хелс Кеа Аг | Стабилизированное соединение гормона роста |
| JP6464145B2 (ja) | 2013-04-05 | 2019-02-06 | ノヴォ・ノルディスク・ヘルス・ケア・アーゲー | 成長ホルモン化合物製剤 |
Family Cites Families (16)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US2175090A (en) * | 1938-06-22 | 1939-10-03 | Lederie Lab Inc | Purification of antibody compositions |
| US3657071A (en) * | 1968-11-12 | 1972-04-18 | Hans Ulrich Bergmeyer | Fractionation of proteins |
| US3749668A (en) * | 1971-05-03 | 1973-07-31 | Rohm & Haas | Water purification with amine oxide resins |
| DE2718325C2 (de) * | 1977-04-25 | 1986-09-25 | Behringwerke Ag, 3550 Marburg | Leucinreiches 3,1-S-α↓2↓-Glykoprotein sowie dessen Verwendung |
| US4204989A (en) * | 1978-12-13 | 1980-05-27 | Merck & Co., Inc. | Isolation of hepatitis B e antigen |
| DE2946458A1 (de) * | 1979-11-17 | 1981-06-11 | Behringwerke Ag, 3550 Marburg | Neues protein pp(pfeil abwaerts)11(pfeil abwaerts) |
| US4778813A (en) * | 1981-07-07 | 1988-10-18 | Buckman Laboratories International, Inc. | Polymeric quaternary ammonium compounds, their preparation and use |
| JPH0738880B2 (ja) * | 1983-06-24 | 1995-05-01 | 東レ株式会社 | エンドトキシン血症治療剤 |
| US4634673A (en) * | 1984-03-28 | 1987-01-06 | Nabisco Brands, Inc. | Enzyme purification process |
| DE3484713D1 (de) * | 1984-09-10 | 1991-07-18 | Toray Industries | Ionenaustausch- oder adsorptionsverfahren. |
| SE462100B (sv) * | 1985-08-08 | 1990-05-07 | Perstorp Ab | Komposition och dess anvaendning i ett tvaa- eller flerfassystem |
| US4677196A (en) * | 1985-09-06 | 1987-06-30 | International Minerals & Chemical Corp. | Purification and activation of proteins from insoluble inclusion bodies |
| DE3608091A1 (de) * | 1986-03-12 | 1987-09-17 | Basf Ag | Verfahren zum isolieren und reinigen von haemin |
| US4771128A (en) * | 1986-10-10 | 1988-09-13 | Cetus Corporation | Method of purifying toxin conjugates using hydrophobic interaction chromatography |
| AU612133B2 (en) * | 1987-02-20 | 1991-07-04 | Natinco Nv | Production of proteins in active forms |
| EP0295859B1 (de) * | 1987-06-15 | 1994-11-17 | Southern Cross Biotech Pty.Ltd. | Herstellung von Proteinen in aktiver Form |
-
1989
- 1989-06-12 US US07/364,846 patent/US5101018A/en not_active Expired - Lifetime
-
1990
- 1990-05-10 EP EP90907861A patent/EP0477198B1/de not_active Expired - Lifetime
- 1990-05-10 WO PCT/US1990/002652 patent/WO1990015876A1/en active IP Right Grant
- 1990-05-10 DE DE90907861T patent/DE69004429T2/de not_active Expired - Fee Related
- 1990-05-10 KR KR1019910701832A patent/KR0178274B1/ko not_active IP Right Cessation
- 1990-05-10 AT AT90907861T patent/ATE96805T1/de not_active IP Right Cessation
- 1990-05-10 HU HU904388A patent/HU209651B/hu not_active IP Right Cessation
- 1990-05-10 AU AU56442/90A patent/AU634547B2/en not_active Ceased
- 1990-05-10 JP JP2507613A patent/JP2957695B2/ja not_active Expired - Fee Related
- 1990-05-10 CA CA002060505A patent/CA2060505C/en not_active Expired - Fee Related
- 1990-05-10 DK DK90907861.0T patent/DK0477198T3/da active
- 1990-05-10 BR BR909007433A patent/BR9007433A/pt not_active Application Discontinuation
- 1990-05-10 ES ES199090907861T patent/ES2046782T3/es not_active Expired - Lifetime
- 1990-05-10 RU SU905010961A patent/RU2075509C1/ru active
- 1990-05-10 HU HU8843Q patent/HUT61053A/hu unknown
Also Published As
| Publication number | Publication date |
|---|---|
| ATE96805T1 (de) | 1993-11-15 |
| AU5644290A (en) | 1991-01-08 |
| CA2060505C (en) | 2001-06-12 |
| HU904388D0 (en) | 1992-04-28 |
| AU634547B2 (en) | 1993-02-25 |
| DE69004429T2 (de) | 1994-03-31 |
| DE69004429D1 (de) | 1993-12-09 |
| WO1990015876A1 (en) | 1990-12-27 |
| KR0178274B1 (ko) | 1999-04-01 |
| EP0477198B1 (de) | 1993-11-03 |
| DK0477198T3 (da) | 1993-11-29 |
| ES2046782T3 (es) | 1994-02-01 |
| RU2075509C1 (ru) | 1997-03-20 |
| HU209651B (en) | 1994-09-28 |
| JPH04505706A (ja) | 1992-10-08 |
| CA2060505A1 (en) | 1990-12-13 |
| BR9007433A (pt) | 1992-06-16 |
| US5101018A (en) | 1992-03-31 |
| HUT61053A (en) | 1992-11-30 |
| EP0477198A1 (de) | 1992-04-01 |
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| LAPS | Cancellation because of no payment of annual fees |